Possible sites of interaction of acute renal failure with amino acid utilization for gluconeogenesis in isolated perfused rat liver.

Experiments were performed to elucidate the mechanisms involved in the enhanced conversion of amino acids to glucose in acute uraemic rats. Increased gluconeogenesis from a mixture of serine, threonine, lysine, glutamate, ornithine and citrulline was confirmed using a non-recirculating perfusion system. Stimulation was concentration dependent, being most pronounced at physiological amino acid concentrations.

A protein inhibitor of mitochondrial adenosine triphosphatase (F1) from Saccharomyces cerevisiae.

A heat-stable protein has been detected in Saccharomyces cerevisiae which inhibits mitochondrial ATPase activity. The protein inhibitor has been isolated from extracts prepared by brief heat treatment of unbroken cell suspensions. The isolated inhibitor is a small basic protein (molecular weight close to 7000, isoelectric proint 9.

[Intracellular localisation of urea-cycle enzymes in liver (author's transl)].

Enzymes of the Krebs-Henseleit urea-cycle were localized by means of differential centrifugation and fractional tissue extraction in rat liver and in human liver. Argininosuccinatlyase (ASAL) and Argininosuccinatsynthetase (ASAS) represent enzymes of the soluble cytoplasmic fraction. Ornithine-ketoacid-transaminase(OKT), carbamyl-phosphate-synthetase (CPS) and ornithine-carbamyl-transferase (OCT) are localized in the mitochondrial and nuclei fractions of the liver cell.

International standard (C.C.I.T.T.) for transmitting biomedical analogue and digital data on the public telephone network.

Analogue transmission of biomedical signals over the public telephone network has advantages from the economic point of view over digitalized transmission. This paper deals with the special problems encountered with the transmission of biomedical signals. Furthermore, the new international transmission standard C.

[Differentiation of cytoplasmatic, mitochondrial and lysosomal enzymes by fractional extraction of rat liver].

Enzymes of extramitochondrial, mitochondrial and lysosomal origin were differentiated by the method of fractional tissue extraction from rat liver. It could be confirmed that soluble enzymes of the extramitochondrial (cytoplasmatic) compartment (glycerine aldehydphosphate-dehydrogenase, argininosuccinate lyase) and soluble enzymes of the mitochondrial matrix can be differentiated easily according to their different intracellular localisation. Additionally, our results emphasize that soluble enzymes of both compartements and marker-enzymes of the lysosomal cell space which are known to be structurally-bound, can be differentiated too.